1INR: Cytokine synthesis

Cytokine synthesis. Determined by X-ray diffraction at 2.0 Å resolution. Released 14 Oct 1996.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Homo sapiens
Chains
1
Atoms
1,114
Mol. weight
18.67 kDa
Released
14 Oct 1996

Explore 1INR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1INR contains 12 α-helices and 0 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 12 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix19-3315
α-helix34-363
α-helix50-567
α-helix61-7111
α-helix72-765
α-helix77-837
α-helix85-873
α-helix88-10518
α-helix113-1153
α-helix119-13012
α-helix133-1419
α-helix143-15614

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Interleukin-10Aprotein160Homo sapiensP22301 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1INR_1 INTERLEUKIN-10 (chains A)
SPGQGTQSENSCTHFPGNLPNMLRDLRDAFSRVKTFFQMKDQLDNLLLKESLLEDFKGYL
GCQALSEMIQFYLEEVMPQAENQDPDIKAHVNSLGENLKTLRLRLRRCHRFLPCENKSKA
VEQVKNAFNKLQEKGIYKAMSEFDIFINYIEAYMTMKIRN

Primary citation

Crystal structure of interleukin 10 reveals an interferon gamma-like fold. Walter, M.R., Nagabhushan, T.L. Biochemistry (1995) 34:12118-12125. DOI 10.1021/bi00038a004 · PubMed

Other PDB entries of the same protein (UniProt P22301 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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